Structural highlights
Function
[NPF_MONEX] May have an important physiological role in neuroregulation.
Publication Abstract from PubMed
The solution structure of neuropeptide F (NPF), from the flatworm (platyhelminthes) Moniezia expansa, has been determined by (1)H NMR spectroscopy at 800 MHz in 60%/40% CD(3)OH/H(2)O. NPF is the most abundant neuropeptide in platyhelminthes. The secondary structure of NPF contains an alpha helix from residues Lys(14) to Ile(31), while the N terminus, consisting of residues Pro(-2) to Asn(13), and the C-terminus, consisting of residues Gly(32) to Phe(36), are in a random conformation. The structure was calculated by a simulated annealing protocol, and the conformational data are compared to the porcine neuropeptide Y (NPY), a peptide hormone and neurotransmitter. The exact function of NPF is unknown, but structural similarity with porcine NPY indicates that its mode of action is similar. These structural data can serve as a starting point in the design of new antiparasitic drugs.
The NMR-derived conformation of neuropeptide F from Moniezia expansa.,Miskolzie M, Kotovych G J Biomol Struct Dyn. 2002 Jun;19(6):991-8. PMID:12023801[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miskolzie M, Kotovych G. The NMR-derived conformation of neuropeptide F from Moniezia expansa. J Biomol Struct Dyn. 2002 Jun;19(6):991-8. PMID:12023801
